Inhibition of amyloid beta-induced synaptotoxicity by a pentapeptide derived from the glycine zipper region of the neurotoxic peptide

2013 ◽  
Vol 34 (12) ◽  
pp. 2805-2814 ◽  
Author(s):  
Christian Peters ◽  
Eduardo J. Fernandez-Perez ◽  
Carlos F. Burgos ◽  
María P. Espinoza ◽  
Carolina Castillo ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Neurotoxic Peptide

Amelioration effects of Cirsium japonicum var. maackii extract/fractions on amyloid beta25–35-induced neurotoxicity in SH-SY5Y cells and identification of the main bioactive compound

2020 ◽  
Vol 11 (11) ◽  
pp. 9651-9661
Author(s):  
Min Jeong Kim ◽  
Ji-Hyun Kim ◽  
Ji Hyun Kim ◽  
Sanghyun Lee ◽  
Eun Ju Cho
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Beta ◽  
Bioactive Compound ◽  
Neurotoxic Peptide ◽  
Cirsium Japonicum ◽  
The Brain

Amyloid beta (Aβ) is a neurotoxic peptide, and the accumulation of Aβ in the brain is the major characteristic of Alzheimer's disease (AD).

Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease

2002 ◽  
Vol 38 ◽  
pp. 37-49 ◽  
Author(s):  
Janelle Nunan ◽  
David H Small
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amyloid Beta ◽  
Alternative Pathway ◽  
Protein A ◽  
Proteolytic Processing ◽  
Gamma Secretase ◽  
Amyloid Beta Protein ◽  
Protein Precursor ◽  
Amyloid Beta Protein Precursor

The proteolytic processing of the amyloid-beta protein precursor plays a key role in the development of Alzheimer's disease. Cleavage of the amyloid-beta protein precursor may occur via two pathways, both of which involve the action of proteases called secretases. One pathway, involving beta- and gamma-secretase, liberates amyloid-beta protein, a protein associated with the neurodegeneration seen in Alzheimer's disease. The alternative pathway, involving alpha-secretase, precludes amyloid-beta protein formation. In this review, we describe the progress that has been made in identifying the secretases and their potential as therapeutic targets in the treatment or prevention of Alzheimer's disease.

Mitochondrial failure precedes amyloid beta plaques deposition in APP transgenic mice

2005 ◽  
Vol 38 (05) ◽  
Author(s):  
A Eckert ◽  
I Scherping ◽  
A Bonert ◽  
S Hauptmann ◽  
F Müller-Spahn ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Amyloid Beta

Rapid, Refined, and Robust Method for Expression, Purification, and Characterization of Recombinant Human Amyloid-beta M1-42

2019 ◽  
Author(s):  
Priya Prakash ◽  
Travis Lantz ◽  
Krupal P. Jethava ◽  
Gaurav Chopra
Keyword(s):  
Amyloid Beta ◽  
Western Blots ◽  
Force Microscopy ◽  
E Coli ◽  
Atomic Force ◽  
Set Up ◽  
Short Time

Amyloid plaques found in the brains of Alzheimer’s disease (AD) patients primarily consists of amyloid beta 1-42 (Ab42). Commercially, Ab42 is synthetized using peptide synthesizers. We describe a robust methodology for expression of recombinant human Ab(M1-42) in Rosetta(DE3)pLysS and BL21(DE3)pLysS competent E. coli with refined and rapid analytical purification techniques. The peptide is isolated and purified from the transformed cells using an optimized set-up for reverse-phase HPLC protocol, using commonly available C18 columns, yielding high amounts of peptide (~15-20 mg per 1 L culture) in a short time. The recombinant Ab(M1-42) forms characteristic aggregates similar to synthetic Ab42 aggregates as verified by western blots and atomic force microscopy to warrant future biological use. Our rapid, refined, and robust technique to purify human Ab(M1-42) can be used to synthesize chemical probes for several downstream in vitro and in vivo assays to facilitate AD research.

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